Research workbench
AlphaFold monomer V2.0 prediction for protein SMY2 (P32909)
Analyse AlphaFold monomer V2.0 prediction for protein SMY2 (P32909) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P32909
- Type
- protein
- Length
- 740 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x4DFa4212bcA4e8C4A6FaABF30918b7cc4486C3Db
- Molecule
- Protein SMY2
- UniProt
- P32909
Structure
1 distinct chain · 25% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein SMY2 | protein | 740 | 25% helix, 3% strand | P32909 |
Compared structures
- 3FMA · Crystal structure of the gyf domain of SMY2 in complex with a proline- rich peptide from… · an experimental structure of the same protein · chain A against A, TM-score 0.11
- 3FMA · Crystal structure of the GYF domain of Smy2 in complex with a proline-rich peptide from… · an experimental structure of the same protein · chain A against A, TM-score 0.11
- 3K3V · Crystal structure the gyf domain of S. cerevisiae SMY2 · an experimental structure of the same protein · chain A against A, TM-score 0.09
- 3K3V · Crystal structure the GYF domain of S. Cerevisiae SMY2 · an experimental structure of the same protein · chain A against A, TM-score 0.09
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P32909
- Elsewhere: UniProt P32909 · AlphaFold DB P32909
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